Intracytoplasmic-membrane development in alphaproteobacteria involves the homolog of the mitochondrial crista-developing protein Mic60
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F23%3A00572376" target="_blank" >RIV/60077344:_____/23:00572376 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/23:00572376 RIV/60076658:12310/23:43906438
Result on the web
<a href="https://www.sciencedirect.com/science/article/abs/pii/S0960982223001999?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/abs/pii/S0960982223001999?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.cub.2023.02.059" target="_blank" >10.1016/j.cub.2023.02.059</a>
Alternative languages
Result language
angličtina
Original language name
Intracytoplasmic-membrane development in alphaproteobacteria involves the homolog of the mitochondrial crista-developing protein Mic60
Original language description
Mitochondrial cristae expand the surface area of respiratory membranes and ultimately allow for the evolutionary scaling of respiration with cell volume across eukaryotes. The discovery of Mic60 homologs among alphaproteobacteria, the closest extant relatives of mitochondria, suggested that cristae might have evolved from bacterial intracytoplasmic membranes (ICMs). Here, we investigated the predicted structure and function of alphaproteobacterial Mic60, and a protein encoded by an adjacent gene Orf52, in two distantly related purple alphaproteobacteria, Rhodobacter sphaeroides and Rhodopseudo-monas palustris. In addition, we assessed the potential physical interactors of Mic60 and Orf52 in R. sphaeroides. We show that the three a helices of mitochondrial Mic60's mitofilin domain, as well as its adjacent membrane-binding amphipathic helix, are present in alphaproteobacterial Mic60. The disrup-tion of Mic60 and Orf52 caused photoheterotrophic growth defects, which are most severe under low light conditions, and both their disruption and overexpression led to enlarged ICMs in both studied alphapro-teobacteria. We also found that alphaproteobacterial Mic60 physically interacts with BamA, the homolog of Sam50, one of the main physical interactors of eukaryotic Mic60. This interaction, responsible for mak-ing contact sites at mitochondrial envelopes, has been conserved in modern alphaproteobacteria despite more than a billion years of evolutionary divergence. Our results suggest a role for Mic60 in photosynthetic ICM development and contact site formation at alphaproteobacterial envelopes. Overall, we provide sup-port for the hypothesis that mitochondrial cristae evolved from alphaproteobacterial ICMs and have there-fore improved our understanding of the nature of the mitochondrial ancestor.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Current Biology
ISSN
0960-9822
e-ISSN
1879-0445
Volume of the periodical
33
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
31
Pages from-to
1099-+
UT code for WoS article
000969910700001
EID of the result in the Scopus database
2-s2.0-85150373308